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Solution structures of the DNA-binding domains of immune-related zinc-finger protein ZFAT.

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Tochio N, Umehara T, Nakabayashi K, Yoneyama M, Tsuda K, Shirouzu M, Koshiba S, Watanabe S, Kigawa T, Sasazuki T, Shirasawa S, Yokoyama S
OpenAccess logo J Struct Funct Genomics 16 55-65 (2015)
Related entries: 2rut, 2ruu, 2ruv, 2ruw, 2rux, 2ruy, 2rv0, 2rv1, 2rv2, 2rv3, 2rv4, 2rv5, 2rv6, 2rv7

Cited: 11 times
EuropePMC logo PMID: 25801860

Abstract

ZFAT is a transcriptional regulator, containing eighteen C2H2-type zinc-fingers and one AT-hook, involved in autoimmune thyroid disease, apoptosis, and immune-related cell survival. We determined the solution structures of the thirteen individual ZFAT zinc-fingers (ZF) and the tandemly arrayed zinc-fingers in the regions from ZF2 to ZF5, by NMR spectroscopy. ZFAT has eight uncommon bulged-out helix-containing zinc-fingers, and six of their structures (ZF4, ZF5, ZF6, ZF10, ZF11, and ZF13) were determined. The distribution patterns of the putative DNA-binding surface residues are different among the ZFAT zinc-fingers, suggesting the distinct DNA sequence preferences of the N-terminal and C-terminal zinc-fingers. Since ZFAT has three to five consecutive tandem zinc-fingers, which may cooperatively function as a unit, we also determined two tandemly arrayed zinc-finger structures, between ZF2 to ZF4 and ZF3 to ZF5. Our NMR spectroscopic analysis detected the interaction between ZF4 and ZF5, which are connected by an uncommon linker sequence, KKIK. The ZF4-ZF5 linker restrained the relative structural space between the two zinc-fingers in solution, unlike the other linker regions with determined structures, suggesting the involvement of the ZF4-ZF5 interfinger linker in the regulation of ZFAT function.

Articles - 2ruz mentioned but not cited (1)

  1. Solution structures of the DNA-binding domains of immune-related zinc-finger protein ZFAT. Tochio N, Umehara T, Nakabayashi K, Yoneyama M, Tsuda K, Shirouzu M, Koshiba S, Watanabe S, Kigawa T, Sasazuki T, Shirasawa S, Yokoyama S. J Struct Funct Genomics 16 55-65 (2015)


Reviews citing this publication (2)

  1. Factors involved in heterologous expression of proteins in E. coli host. Pouresmaeil M, Azizi-Dargahlou S. Arch Microbiol 205 212 (2023)
  2. Zinc finger structure determination by NMR: Why zinc fingers can be a handful. Neuhaus D. Prog Nucl Magn Reson Spectrosc 130-131 62-105 (2022)

Articles citing this publication (8)

  1. SARS-CoV-2 Virion Stabilization by Zn Binding. Morante S, La Penna G, Rossi G, Stellato F. Front Mol Biosci 7 222 (2020)
  2. ZFAT binds to centromeres to control noncoding RNA transcription through the KAT2B-H4K8ac-BRD4 axis. Ishikura S, Nakabayashi K, Nagai M, Tsunoda T, Shirasawa S. Nucleic Acids Res 48 10848-10866 (2020)
  3. Engineering protein activity into off-the-shelf DNA devices. Sekhon H, Loh SN. Cell Rep Methods 2 100202 (2022)
  4. Structural Insights into c-Myc-interacting Zinc Finger Protein-1 (Miz-1) Delineate Domains Required for DNA Scanning and Sequence-specific Binding. Bédard M, Roy V, Montagne M, Lavigne P. J Biol Chem 292 3323-3340 (2017)
  5. The transcriptional regulator Zfat is essential for maintenance and differentiation of the adipocytes. Ishikura S, Nagai M, Tsunoda T, Nishi K, Tanaka Y, Koyanagi M, Shirasawa S. J Cell Biochem 122 626-638 (2021)
  6. CENP-B promotes the centromeric localization of ZFAT to control transcription of noncoding RNA. Ishikura S, Yoshida K, Hashimoto S, Nakabayashi K, Tsunoda T, Shirasawa S. J Biol Chem 297 101213 (2021)
  7. Zfat expression in ZsGreen reporter gene knock‑in mice: Implications for a novel function of Zfat in definitive erythropoiesis. Tsunoda T, Doi K, Ishikura S, Luo H, Nishi K, Matsuzaki H, Koyanagi M, Tanaka Y, Okamura T, Shirasawa S. Int J Mol Med 42 2595-2603 (2018)
  8. Death domain-associated protein DAXX regulates noncoding RNA transcription at the centromere through the transcription regulator ZFAT. Ishikura S, Yoshida K, Tsunoda T, Shirasawa S. J Biol Chem 298 102528 (2022)


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